rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2003-1-3
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pubmed:abstractText |
Polarized cells contain numerous membrane domains, but it is unclear how the formation of these domains is coordinated to create a single integrated cell architecture. Genetic screens of Drosophila melanogaster embryos have identified three complexes, each containing one of the PDZ domain proteins--Stardust (Sdt), Bazooka (Baz) and Scribble (Scrib)--that control epithelial polarity and formation of zonula adherens. We find that these complexes can be ordered into a single regulatory hierarchy that is initiated by cell adhesion-dependent recruitment of the Baz complex to the zonula adherens. The Scrib complex represses apical identity along basolateral surfaces by antagonizing Baz-initiated apical polarity. The Sdt-containing Crb complex is recruited apically by the Baz complex to counter antagonistic Scrib activity. Thus, a finely tuned balance between Scrib and Crb complex activity sets the limits of the apical and basolateral membrane domains and positions cell junctions. Our data suggest a model in which the maturation of epithelial cell polarity is driven by integration of the sequential activities of PDZ-based protein complexes.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Phosphate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Scribble protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/bazooka protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/sdt protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
53-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12510194-Alleles,
pubmed-meshheading:12510194-Animals,
pubmed-meshheading:12510194-Binding Sites,
pubmed-meshheading:12510194-Carrier Proteins,
pubmed-meshheading:12510194-Cell Polarity,
pubmed-meshheading:12510194-Drosophila Proteins,
pubmed-meshheading:12510194-Drosophila melanogaster,
pubmed-meshheading:12510194-Embryo, Nonmammalian,
pubmed-meshheading:12510194-Epithelial Cells,
pubmed-meshheading:12510194-Guanylate Kinase,
pubmed-meshheading:12510194-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:12510194-Membrane Proteins,
pubmed-meshheading:12510194-Membrane Transport Proteins,
pubmed-meshheading:12510194-Nucleoside-Phosphate Kinase
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pubmed:year |
2003
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pubmed:articleTitle |
Integrated activity of PDZ protein complexes regulates epithelial polarity.
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pubmed:affiliation |
Department of Genetics and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA. bilder@socrates.berkeley.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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